Hemoglobin is a protein in red blood cells responsible for transporting oxygen from the lungs to the rest of the body and carbon dioxide back to the lungs. It binds with oxygen in areas of high concentration like the lungs and releases it in tissues where oxygen levels are low.
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Hemoglobin consists of four subunits, each containing an iron atom that binds to an oxygen molecule.
Each hemoglobin molecule can carry up to four oxygen molecules.
The binding and release of oxygen by hemoglobin are influenced by factors such as pH, carbon dioxide levels, and temperature.
Hemoglobin also plays a role in buffering blood pH by binding to hydrogen ions.
Anemia is often caused by low levels of hemoglobin, leading to reduced oxygen transport capacity.
Review Questions
What is the primary function of hemoglobin in red blood cells?
How many oxygen molecules can one hemoglobin molecule transport at maximum capacity?
What factors influence the binding affinity of hemoglobin for oxygen?
Related terms
Red Blood Cells (Erythrocytes): Specialized cells that contain hemoglobin and transport oxygen and carbon dioxide throughout the body.
Oxyhemoglobin: The form of hemoglobin bound to oxygen, primarily found in arterial blood after leaving the lungs.
Bohr Effect: The physiological phenomenon where decreases in blood pH or increases in carbon dioxide concentration reduce hemoglobin's affinity for oxygen.